FLIF_BUCAI
ID FLIF_BUCAI Reviewed; 545 AA.
AC P57175;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Flagellar M-ring protein;
GN Name=fliF; OrderedLocusNames=BU073;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: The M ring may be actively involved in energy transduction.
CC {ECO:0000250}.
CC -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC organelle and consists of four rings (L,P,S, and M) mounted on a
CC central rod. The M ring is integral to the inner membrane of the cell
CC and may be connected to the flagellar rod via the S ring. The S
CC (supramembrane ring) lies just distal to the M ring. The L and P rings
CC lie in the outer membrane and the periplasmic space, respectively (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FliF family. {ECO:0000305}.
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DR EMBL; BA000003; BAB12793.1; -; Genomic_DNA.
DR RefSeq; NP_239907.1; NC_002528.1.
DR RefSeq; WP_010895926.1; NC_002528.1.
DR AlphaFoldDB; P57175; -.
DR SMR; P57175; -.
DR STRING; 107806.10038758; -.
DR PRIDE; P57175; -.
DR EnsemblBacteria; BAB12793; BAB12793; BAB12793.
DR KEGG; buc:BU073; -.
DR PATRIC; fig|107806.10.peg.79; -.
DR eggNOG; COG1766; Bacteria.
DR HOGENOM; CLU_028108_1_0_6; -.
DR OMA; NYEVNRI; -.
DR Proteomes; UP000001806; Chromosome.
DR GO; GO:0009431; C:bacterial-type flagellum basal body, MS ring; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR013556; Flag_M-ring_C.
DR InterPro; IPR000067; FlgMring_FliF.
DR InterPro; IPR006182; FliF_N_dom.
DR InterPro; IPR043427; YscJ/FliF.
DR PANTHER; PTHR30046; PTHR30046; 1.
DR PANTHER; PTHR30046:SF0; PTHR30046:SF0; 1.
DR Pfam; PF01514; YscJ_FliF; 1.
DR Pfam; PF08345; YscJ_FliF_C; 1.
DR PIRSF; PIRSF004862; FliF; 1.
DR PRINTS; PR01009; FLGMRINGFLIF.
DR TIGRFAMs; TIGR00206; fliF; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..545
FT /note="Flagellar M-ring protein"
FT /id="PRO_0000180878"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 545 AA; 62605 MW; 608249E227AF6B80 CRC64;
MNFSTIEESV LKEKKKFNNF LSGFLKNSRF LIILLTAAAI TAVSISVWIK SPEYQVLYNH
LSNEDRGSII NELNEMKIPY QFTDSDGPIL VPKDKVYEIR LRLAENNLPR GGSIGFELLD
KEKFGISQYN EQINYHRALE GELARTIKKI NSVKNARIHI AFSKSSLFLQ DKKKSSASII
LELQPGRNLN TGQINAIMHL ISSSISDLPV ENITIVDQSG KLLNQTSVEY DQVNDSQFKY
TEEIETRYRN RIKNILEPLV GIGNIYAQVT AQIDFNAQEK TQEKYSPNSD HKNQSIRSHQ
IIIHNEIEKS NIQEETPIPL SNSNNHVYFN NNIKNSKNLK NNYIPVDSKI NRDNTVNYEL
NHSVSHTKMN IGEIKRLSAA VIVNFSKDKN GKFVPLSTQK IKNIEHLIRE AIGYSKARGD
SVHLVNASFA KYDQKIPVHI NHINTFRKSN FLYNFAPWFC SFALLFLLLK KYICPFSKNN
TFQNTIPVQE KKSIDTRNII EKNTFQVDLQ NNTNTDKLIH KICNISNQNP RTIALIIRQW
MSDKI